Structure of PDB 5koi Chain E

Receptor sequence
>5koiE (length=271) Species: 262698 (Brucella abortus bv. 1 str. 9-941) [Search protein sequence]
EGLMQGKRGLIMGVANNHSLAWGIAKQLAAQGAELAFTYQGDALGKRVKP
LAEQVGSDFVLPCDVEDIATVDAVFEEIEKKWGGLDFLVHAIGFSDKTEL
KGRYADVTTRENFSRTMVISAYSFTEVAQRAEKLMKDGGSILTLTYGGST
RTIPNYNVMGVAKAALEAMVRYLAADYGPQGIRVNAISAGPVRTLAGAGI
GDARAIFSYQRRNSPLRRTVDIDDVGKSAVYLLSDLSSGVTGEIHFVDSG
YNIVSMPTLEELKSSDSERGE
3D structure
PDB5koi Crystal Structure of a Possible Enoyl-(acyl-carrier-protein) Reductase from Brucella melitensis
ChainE
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y147 Y157 K164
Catalytic site (residue number reindexed from 1) Y146 Y156 K163
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD E G14 A16 S20 L21 Q41 D65 V66 A92 I93 G94 I120 L145 T146 Y147 K164 A190 P192 V193 T195 A197 G13 A15 S19 L20 Q40 D64 V65 A91 I92 G93 I119 L144 T145 Y146 K163 A189 P191 V192 T194 A196
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5koi, PDBe:5koi, PDBj:5koi
PDBsum5koi
PubMed
UniProtQ57A95

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